食品科学 ›› 2018, Vol. 39 ›› Issue (14): 9-15.doi: 10.7506/spkx1002-6630-201814002

• 食品化学 • 上一篇    下一篇

生物解离大豆乳状液中蛋白质结构特征分析

王立敏,陈思,丁俭,齐宝坤,王中江,江连洲,隋晓楠,Olga Olegovna Babich,李杨*   

  1. (东北农业大学食品学院,黑龙江?哈尔滨 150030)
  • 出版日期:2018-07-25 发布日期:2018-07-16
  • 基金资助:
    “十三五”国家重点研发计划重点专项(2016YFD0401402);霍英东教育基金项目(151033)

Structural Characteristics of Protein Emulsion Formed during Enzyme-Assisted Aqueous Extraction of Soybean Oil

WANG Limin, CHEN Si, DING Jian, QI Baokun, WANG Zhongjiang, JIANG Lianzhou, SUI Xiaonan, Olga Olegovna Babich, LI Yang*   

  1. (College of Food Science and technology, Northeast Agricultural University, Harbin 150030, China)
  • Online:2018-07-25 Published:2018-07-16

摘要: 以不同酶解时间(1、2、3 h)、不同酶添加量(1%、2%)生物解离大豆过程中形成的乳状液蛋白质为研究对象,采用扫描电子显微镜、乳化活性指数(emulsion activity index,EAI)和乳化稳定性指数(emulsion stability index,ESI)、表面疏水性、氨基酸分析及傅里叶变换红外光谱等表征乳状液蛋白质/多肽表面性质及结构特征。结果显示:随着酶解的进行,乳状液中蛋白质由致密有序的网状结构变为疏松、多孔结构,EAI和ESI呈逐渐降低趋势;同时,疏水性氨基酸比例增多,表面疏水性指数(S0)下降,由于疏水性残基之间通过疏水相互作用发生聚集,对蛋白质的疏水区域产生屏蔽作用,导致S0下降;傅里叶变换红外光谱结果显示,随着酶解程度的增加,α-螺旋、β-折叠结构减少,无规则卷曲结构增加,表明酶解过程中引起了分子间作用力变化,导致乳状液蛋白质的构象变化。上述结果是酶解过程中乳状液失稳的主要原因之一,为生物解离乳状液破乳机制提供理论支持。

关键词: 乳状液蛋白质, 表面疏水性, 氨基酸分析, 傅里叶变换红外光谱, 结构特征

Abstract: In this study, we evaluated the protein emulsions formed during the enzyme-assisted aqueous extraction of soybean oil under different conditions of enzyme dosage (1% and 2%) and hydrolysis time (1, 2 and 3 h). The surface properties and structural characteristics of the emulsion protein/polypeptide were characterized by scanning electron microscopy, emulsion activity index (EAI), emulsion stability index (ESI), surface hydrophobicity (S0), amino acid analysis and Fourier transform infrared spectroscopy. The results showed that as the enzymatic hydrolysis proceeded, the protein in the emulsions changed from a dense and orderly network structure to a loose porous structure, the EAI and ESI gradually decreased; in addition, the proportion of hydrophobic amino acid increased and surface hydrophobicity (S0) decreased due to aggregation of the hydrophobic residues through their mutual interaction, blocking the hydrophobic groups. Fourier transform infrared spectra showed that the proportions of α-helix and β-sheet structure were reduced while the proportion of irregular structure increased with increasing degree of hydrolysis, indicating that the changes in intermolecular force caused by the enzymatic hydrolysis led to conformational changes of protein in the emulsions. The above results can largely emulsion instability during the enzymatic hydrolysis, which will provide theoretical support for understanding the mechanism of emulsion demulsification during the enzyme-assisted aqueous extraction of soybean oil.

Key words: protein emulsion, surface hydrophobicity (S0), amino acid analysis, Fourier transform infrared spectroscopy, structure characteristics

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